|
Name |
Accession |
Description |
Interval |
E-value |
| 2am3keto_CoA |
TIGR01822 |
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ... |
27-418 |
0e+00 |
|
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and bacterial (almost exclusively Proteobacterial) 2-amino-3-ketobutyrate--CoA ligase, now called glycine C-acetyltransferase. This enzyme can act in threonine catabolism. The closest homolog from Bacillus subtilis, and sequences like it, may be functionally equivalent but were not included in the model because of difficulty in finding reports of function. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130881 [Multi-domain] Cd Length: 393 Bit Score: 724.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 27 LRGILEGELEGIRGAGTWKSERVITSRQGPHIRV-DGvsGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFI 105
Cdd:TIGR01822 1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG--REVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 106 CGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLE 185
Cdd:TIGR01822 79 CGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 186 AKLQEAQKH--RLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 263
Cdd:TIGR01822 159 AQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 264 GKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISG 343
Cdd:TIGR01822 239 GKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKP 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7657118 344 ASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGAL 418
Cdd:TIGR01822 319 ADHPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHTEEQLDRAVEAFTRIGRELGVI 393
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
31-418 |
0e+00 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 654.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGvSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQS 110
Cdd:PRK06939 9 LREELEEIKAEGLYKEERVITSPQGADITVAD-GKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 111 IHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQE 190
Cdd:PRK06939 88 LHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 191 AQK--HRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALG 268
Cdd:PRK06939 168 AKEagARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 269 GASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPI 348
Cdd:PRK06939 248 GASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTLGPGEHPI 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 349 CPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGAL 418
Cdd:PRK06939 328 IPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
31-413 |
0e+00 |
|
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439926 [Multi-domain] Cd Length: 385 Bit Score: 542.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGvsGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQS 110
Cdd:COG0156 5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDG--REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 111 IHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQE 190
Cdd:COG0156 83 LHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 191 AQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGA 270
Cdd:COG0156 163 ARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKAL-GS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 271 SGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICP 350
Cdd:COG0156 242 SGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVP 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7657118 351 VMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGR 413
Cdd:COG0156 322 VIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
67-412 |
2.63e-158 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 450.09 E-value: 2.63e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 67 ILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALL 146
Cdd:cd06454 3 VLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 147 TPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEA-QKHRLRLVATDGAFSMDGDIAPLQEICCLASRYG 225
Cdd:cd06454 83 GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 226 ALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGC 305
Cdd:cd06454 163 AILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 306 ASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGF-TISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKG 384
Cdd:cd06454 242 ALAALEVLQGGPERRERLQENVRYLRRGLKELGFpVGGSPSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPRG 321
|
330 340
....*....|....*....|....*...
gi 7657118 385 KARIRVQISAVHSEEDIDRCVEAFVEVG 412
Cdd:cd06454 322 TARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
67-408 |
1.67e-59 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 197.53 E-value: 1.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 67 ILNFCANNYLGLSShPEVIQAGLQALEefgaglSSVRFICGTQSIHKNLEAKIARFH--------QREDAILYPSCYDAN 138
Cdd:pfam00155 3 KINLGSNEYLGDTL-PAVAKAEKDALA------GGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAGAN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 139 AGLFEALL-TPEDAVLSDELNHASIIDGIRLCKAHKYRYR-------HLDMADLEAKLQEAQKhrlrLVATDGAFSMDGD 210
Cdd:pfam00155 76 IEALIFLLaNPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK----VVLHTSPHNPTGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 211 IAPLQEICCLAS---RYGALVFMDECHATGFLGPTGRGTDeLLGVMDQV-TIINSTLGKALG--GASGGYTTGPGPLVSL 284
Cdd:pfam00155 152 VATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPnLLVVGSFSKAFGlaGWRVGYILGNAAVISQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 285 LRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMAD 364
Cdd:pfam00155 231 LRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 7657118 365 DMLKR-GIFVIGFSYPVVPkgkARIRVQISAvHSEEDIDRCVEAF 408
Cdd:pfam00155 311 VLLEEvGVYVTPGSSPGVP---GWLRITVAG-GTEEELEELLEAI 351
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| 2am3keto_CoA |
TIGR01822 |
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ... |
27-418 |
0e+00 |
|
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and bacterial (almost exclusively Proteobacterial) 2-amino-3-ketobutyrate--CoA ligase, now called glycine C-acetyltransferase. This enzyme can act in threonine catabolism. The closest homolog from Bacillus subtilis, and sequences like it, may be functionally equivalent but were not included in the model because of difficulty in finding reports of function. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130881 [Multi-domain] Cd Length: 393 Bit Score: 724.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 27 LRGILEGELEGIRGAGTWKSERVITSRQGPHIRV-DGvsGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFI 105
Cdd:TIGR01822 1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG--REVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 106 CGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLE 185
Cdd:TIGR01822 79 CGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 186 AKLQEAQKH--RLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 263
Cdd:TIGR01822 159 AQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 264 GKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISG 343
Cdd:TIGR01822 239 GKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKP 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7657118 344 ASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGAL 418
Cdd:TIGR01822 319 ADHPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHTEEQLDRAVEAFTRIGRELGVI 393
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
31-418 |
0e+00 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 654.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGvSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQS 110
Cdd:PRK06939 9 LREELEEIKAEGLYKEERVITSPQGADITVAD-GKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 111 IHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQE 190
Cdd:PRK06939 88 LHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 191 AQK--HRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALG 268
Cdd:PRK06939 168 AKEagARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 269 GASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPI 348
Cdd:PRK06939 248 GASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTLGPGEHPI 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 349 CPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGAL 418
Cdd:PRK06939 328 IPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
31-413 |
0e+00 |
|
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439926 [Multi-domain] Cd Length: 385 Bit Score: 542.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGvsGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQS 110
Cdd:COG0156 5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDG--REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 111 IHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQE 190
Cdd:COG0156 83 LHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 191 AQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGA 270
Cdd:COG0156 163 ARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKAL-GS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 271 SGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICP 350
Cdd:COG0156 242 SGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVP 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7657118 351 VMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGR 413
Cdd:COG0156 322 VIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
67-412 |
2.63e-158 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 450.09 E-value: 2.63e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 67 ILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALL 146
Cdd:cd06454 3 VLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 147 TPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEA-QKHRLRLVATDGAFSMDGDIAPLQEICCLASRYG 225
Cdd:cd06454 83 GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 226 ALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGC 305
Cdd:cd06454 163 AILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 306 ASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGF-TISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKG 384
Cdd:cd06454 242 ALAALEVLQGGPERRERLQENVRYLRRGLKELGFpVGGSPSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPRG 321
|
330 340
....*....|....*....|....*...
gi 7657118 385 KARIRVQISAVHSEEDIDRCVEAFVEVG 412
Cdd:cd06454 322 TARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
48-408 |
5.39e-133 |
|
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. This model represents 8-amino-7-oxononanoate synthase, the BioF protein of biotin biosynthesis. This model is based on a careful phylogenetic analysis to separate members of this family from 2-amino-3-ketobutyrate and other related pyridoxal phosphate-dependent enzymes. In several species, including Staphylococcus and Coxiella, a candidate 8-amino-7-oxononanoate synthase is confirmed by location in the midst of a biotin biosynthesis operon but scores below the trusted cutoff of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 273303 [Multi-domain] Cd Length: 360 Bit Score: 386.24 E-value: 5.39e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 48 RVITSRQGPHIRVDGVSggILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQRED 127
Cdd:TIGR00858 1 RPLDRGPGPEVVRDGRR--LLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 128 AILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSM 207
Cdd:TIGR00858 79 ALLFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 208 DGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVM-DQVTIINSTLGKALGGAsGGYTTGPGPLVSLLR 286
Cdd:TIGR00858 159 DGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKpEPVDIQVGTLSKALGSY-GAYVAGSQALIDYLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 287 QRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDM 366
Cdd:TIGR00858 238 NRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEEL 317
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 7657118 367 LKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAF 408
Cdd:TIGR00858 318 QQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
31-412 |
2.74e-121 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 357.16 E-value: 2.74e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGVSggILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQS 110
Cdd:PRK05958 7 LEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRR--MLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 111 IHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQE 190
Cdd:PRK05958 85 AHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 191 AQKHRlRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALgG 269
Cdd:PRK05958 165 WRAGR-ALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLaGEPDVILVGTLGKAL-G 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 270 ASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPIC 349
Cdd:PRK05958 243 SSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSAIQ 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7657118 350 PVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVG 412
Cdd:PRK05958 323 PLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
|
|
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
70-413 |
1.69e-103 |
|
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273820 [Multi-domain] Cd Length: 402 Bit Score: 312.43 E-value: 1.69e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 70 FCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDAN-AGLFE-ALLT 147
Cdd:TIGR01821 50 WCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANdATLATlAKII 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 148 PEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGAL 227
Cdd:TIGR01821 130 PGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGAL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 228 VFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCAS 307
Cdd:TIGR01821 210 TYLDEVHAVGLYGPRGGGIAERDGLMHRIDIIEGTLAKAF-GVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGAT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 308 KALDLLMGSNTIVQSMAAKTQRFRSKMEAAGF-TISGASHpICPVMLGDARLASRMADDML-KRGIFVIGFSYPVVPKGK 385
Cdd:TIGR01821 289 ASIRHLKESQDLRRAHQENVKRLKNLLEALGIpVIPNPSH-IVPVIIGDAALCKKVSDLLLnKHGIYVQPINYPTVPRGT 367
|
330 340
....*....|....*....|....*...
gi 7657118 386 ARIRVQISAVHSEEDIDRCVEAFVEVGR 413
Cdd:TIGR01821 368 ERLRITPTPAHTDKMIDDLVEALLLVWD 395
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
53-411 |
2.36e-92 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 284.44 E-value: 2.36e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 53 RQGPHIRVDGVSGG--ILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAIL 130
Cdd:PRK13392 32 GRFPRARDHGPDGPrrVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 131 YPSCYDANAGLFEAL--LTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMD 208
Cdd:PRK13392 112 FTSGYVSNDAALSTLgkLLPGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASVDPDRPKLIAFESVYSMD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 209 GDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQR 288
Cdd:PRK13392 192 GDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRIDMIQGTLAKAF-GCLGGYIAASADLIDFVRSF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 289 ARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLK 368
Cdd:PRK13392 271 APGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRVAALKAKLNANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMS 350
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 7657118 369 R-GIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEV 411
Cdd:PRK13392 351 EhGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAI 394
|
|
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
68-416 |
2.64e-65 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 216.55 E-value: 2.64e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 68 LNFCANNYLGLSSH-----PEVIQAglqaLEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLF 142
Cdd:PLN02483 103 LNLGSYNYLGFAAAdeyctPRVIES----LKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTII 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 143 EALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEA------QKHRLR---LVATDGAFSMDGDIAP 213
Cdd:PLN02483 179 PALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQiaegqpRTHRPWkkiIVIVEGIYSMEGELCK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 214 LQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPY 292
Cdd:PLN02483 259 LPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVdPADVDIMMGTFTKSF-GSCGGYIAGSKELIQYLKRTCPAH 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 293 LFSNSLPPAVVGCASKALDLLM---GSNTIVQSMAA---KTQRFRSKMEAAGFTISGAS-HPICPVML-GDARLA--SRm 362
Cdd:PLN02483 338 LYATSMSPPAVQQVISAIKVILgedGTNRGAQKLAQireNSNFFRSELQKMGFEVLGDNdSPVMPIMLyNPAKIPafSR- 416
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 7657118 363 adDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHG 416
Cdd:PLN02483 417 --ECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVG 468
|
|
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
62-408 |
3.67e-60 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 202.60 E-value: 3.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 62 GVSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGL 141
Cdd:PLN02955 99 GRFKKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 142 FEAL-------------LTPED-AVLSDELNHASIIDGIRLCK----AHKYRYRHLDMADLEAKLQEAQKHRlRLVATDG 203
Cdd:PLN02955 179 MVAIgsvasllaasgkpLKNEKvAIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHLNSLLSSCKMKR-KVVVTDS 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 204 AFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKAlGGASGGYTTGPGPLVS 283
Cdd:PLN02955 258 LFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKA-AGCHGGFIACSKKWKQ 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 284 LLRQRARPYLFSNSLPPAVVGCASKAldLLMGSNTIVQSMAAkTQRFRSKMEAAGFTISGashPICPVMLGDARLASRMA 363
Cdd:PLN02955 337 LIQSRGRSFIFSTAIPVPMAAAAYAA--VVVARKEKWRRKAI-WERVKEFKALSGVDISS---PIISLVVGNQEKALKAS 410
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 7657118 364 DDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAF 408
Cdd:PLN02955 411 RYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
67-408 |
1.67e-59 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 197.53 E-value: 1.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 67 ILNFCANNYLGLSShPEVIQAGLQALEefgaglSSVRFICGTQSIHKNLEAKIARFH--------QREDAILYPSCYDAN 138
Cdd:pfam00155 3 KINLGSNEYLGDTL-PAVAKAEKDALA------GGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAGAN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 139 AGLFEALL-TPEDAVLSDELNHASIIDGIRLCKAHKYRYR-------HLDMADLEAKLQEAQKhrlrLVATDGAFSMDGD 210
Cdd:pfam00155 76 IEALIFLLaNPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK----VVLHTSPHNPTGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 211 IAPLQEICCLAS---RYGALVFMDECHATGFLGPTGRGTDeLLGVMDQV-TIINSTLGKALG--GASGGYTTGPGPLVSL 284
Cdd:pfam00155 152 VATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPnLLVVGSFSKAFGlaGWRVGYILGNAAVISQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 285 LRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMAD 364
Cdd:pfam00155 231 LRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 7657118 365 DMLKR-GIFVIGFSYPVVPkgkARIRVQISAvHSEEDIDRCVEAF 408
Cdd:pfam00155 311 VLLEEvGVYVTPGSSPGVP---GWLRITVAG-GTEEELEELLEAI 351
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
49-411 |
2.20e-54 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 187.64 E-value: 2.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 49 VITSRQGPHIRVDGVSggILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDA 128
Cdd:PLN02822 95 VLESAAGPHTIINGKD--VVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 129 ILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQE-------AQKHRlRLVAT 201
Cdd:PLN02822 173 ILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKltaenkrKKKLR-RYIVV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 202 DGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALGGAsGGYTTGPGP 280
Cdd:PLN02822 252 EAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHALATE-GGFCTGSAR 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 281 LVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIV----QSMAAKTQRFRSKMEaagftISGASHPICPVML--- 353
Cdd:PLN02822 331 VVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLaklkENIALLHKGLSDIPG-----LSIGSNTLSPIVFlhl 405
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7657118 354 --------GDARLASRMADDMLKR-GIFVIGFSYPVVPKGK--ARIRVQISAVHSEEDIDRCVEAFVEV 411
Cdd:PLN02822 406 ekstgsakEDLSLLEHIADRMLKEdSVLVVVSKRSTLDKCRlpVGIRLFVSAGHTESDILKASESLKRV 474
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
47-411 |
4.78e-52 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 179.43 E-value: 4.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 47 ERVITSRQGPHIRVDGVSG-GILNFCANNYLGLSSHPEVIQAGLQALEEFGAGL--SSVrFICGTQSIHKnLEAKIARFH 123
Cdd:PRK07179 35 ERVNKNWNGKHLVLGKTPGpDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSLvmSAV-FLHDDSPKPQ-FEKKLAAFT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 124 QREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEaqkHRLRLVATDG 203
Cdd:PRK07179 113 GFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIER---HGPGIIVVDS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 204 AFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALGGaSGGYTTGPGPLVS 283
Cdd:PRK07179 190 VYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAG-RAGIITCPRELAE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 284 LLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHpICPVMLGDARLASRMA 363
Cdd:PRK07179 269 YVPFVSYPAIFSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSELGYNIRSESQ-IIALETGSERNTEVLR 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 7657118 364 DDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDR----CVEAFVEV 411
Cdd:PRK07179 348 DALEERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRvlevCREARDEV 399
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
68-407 |
6.22e-43 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 155.06 E-value: 6.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 68 LNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLT 147
Cdd:PLN03227 1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 148 PEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADL----------EAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEI 217
Cdd:PLN03227 81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLrrvleqvraqDVALKRKPTDQRRFLVVEGLYKNTGTLAPLKEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 218 CCLASRYGALVFMDECHATGFLGPTGRGTDELLGV--MDQVTIINSTLGKALGGAsGGYTTGPGPLVSLLRQRARPYLFS 295
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSV-GGMTVGSEEVVDHQRLSGSGYCFS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 296 NSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRS-----------KMEAAGFTISGASHPICPVMLGDAR------- 357
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGPQLLNRLHDSIANLYStltnsshpyalKLRNRLVITSDPISPIIYLRLSDQEatrrtde 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 7657118 358 --LASRMADDMLKRGIFVI--GFSYPVVPKGKAR--IRVQISAVHSEEDIDRCVEA 407
Cdd:PLN03227 320 tlILDQIAHHSLSEGVAVVstGGHVKKFLQLVPPpcLRVVANASHTREDIDKLLTV 375
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
50-417 |
8.81e-43 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 154.75 E-value: 8.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 50 ITSRQGPHIRVDGVSGG-ILNFCANNYLGLSSHPEVIQAGLQALEEFGA-GLSSVRFICGTQsIHKNLEAKIARFHQREd 127
Cdd:PRK07505 30 LTVGEREGILITLADGHtFVNFVSCSYLGLDTHPAIIEGAVDALKRTGSlHLSSSRTRVRSQ-ILKDLEEALSELFGAS- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 128 AILYPSCYDANAGLFEAL----LTPEDAVLS--DELNHASIIDGIRLCkAHKYRYRHLDMADLEAKLQEAQKHRLRLVAT 201
Cdd:PRK07505 108 VLTFTSCSAAHLGILPLLasghLTGGVPPHMvfDKNAHASLNILKGIC-ADETEVETIDHNDLDALEDICKTNKTVAYVA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 202 DGAFSMdGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRG--TDELLGVMDQVTIINSTLGKALGGASGGYTTGPG 279
Cdd:PRK07505 187 DGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyvRSELDYRLNERTIIAASLGKAFGASGGVIMLGDA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 280 PLVSLLRQRARPYLFSNSLPPAVVGCASKALDL-LMGSNTIVQ-SMAAKTQRFRSKMEAagfTISGASHPICPVMLGDAR 357
Cdd:PRK07505 266 EQIELILRYAGPLAFSQSLNVAALGAILASAEIhLSEELDQLQqKLQNNIALFDSLIPT---EQSGSFLPIRLIYIGDED 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 358 LASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGA 417
Cdd:PRK07505 343 TAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKEILDEGLA 402
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
68-402 |
3.39e-24 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 102.94 E-value: 3.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 68 LNFCANNYLGLSSHPEV---IQAGLQAL------EEFGAGLSsvRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDAN 138
Cdd:PRK05937 7 IDFVTNDFLGFSRSDTLvheVEKRYRLYcrqfphAQLGYGGS--RAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMAN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 139 AGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLR--LVATDGAFSMDGDIAPLQE 216
Cdd:PRK05937 85 LGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFGriFIFVCSVYSFKGTLAPLEQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 217 ICCLASRYGALVFMDECHATGFLGPTGRGTDELLGvMDQVTIINSTLGKALGgasggyTTGPGPLVSL-----LRQRARP 291
Cdd:PRK05937 165 IIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLG-YENFYAVLVTYSKALG------SMGAALLSSSevkqdLMLNSPP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 292 YLFSNSLPPAVVGCASKALDLLMGSNTIvqsmaAKTQRFRSKMEAAGFTISGASHPICPVMLGDarLASRMADDMLKRGI 371
Cdd:PRK05937 238 LRYSTGLPPHLLISIQVAYDFLSQEGEL-----ARKQLFRLKEYFAQKFSSAAPGCVQPIFLPG--ISEQELYSKLVETG 310
|
330 340 350
....*....|....*....|....*....|.
gi 7657118 372 FVIGFsypVVPKGKARIRVQISAVHSEEDID 402
Cdd:PRK05937 311 IRVGV---VCFPTGPFLRVNLHAFNTEDEVD 338
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
112-277 |
2.52e-16 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 76.27 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 112 HKNLEAKIARFHQ--REDAILYPSCYDANAGLFEALLTPEDAVLSDELNHAS---IIDGIRLCKAHKYRYRHLDMADLEA 186
Cdd:cd01494 2 LEELEEKLARLLQpgNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrywVAAELAGAKPVPVPVDDAGYGGLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 187 KLQEAQKHRLR--LVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGflgptGRGTDELLGVMDQVTIINSTLG 264
Cdd:cd01494 82 AILEELKAKPNvaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG-----ASPAPGVLIPEGGADVVTFSLH 156
|
170
....*....|...
gi 7657118 265 KALGGASGGYTTG 277
Cdd:cd01494 157 KNLGGEGGGVVIV 169
|
|
| OAT_like |
cd00610 |
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ... |
76-411 |
1.02e-10 |
|
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to ornithine aminotransferase, acetylornithine aminotransferase, alanine-glyoxylate aminotransferase, dialkylglycine decarboxylase, 4-aminobutyrate aminotransferase, beta-alanine-pyruvate aminotransferase, adenosylmethionine-8-amino-7-oxononanoate aminotransferase, and glutamate-1-semialdehyde 2,1-aminomutase. All the enzymes belonging to this family act on basic amino acids and their derivatives are involved in transamination or decarboxylation.
Pssm-ID: 99735 [Multi-domain] Cd Length: 413 Bit Score: 62.97 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 76 LGLSSHPEVIQAGLQALEEFGAGLSSVRF-ICGTQSIhknlEA--KIARFHQREDAILypSCYDANAG-LFEAL-LTPED 150
Cdd:cd00610 73 LGFFYNEPAVELAELLLALTPEGLDKVFFvNSGTEAV----EAalKLARAYTGRKKII--SFEGAYHGrTLGALsLTGSK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 151 A---VLSDELNHASIIDGirlckAHKYRYRHLDMADLEAkLQEAQKHRLRLVAtdgAFSMD------GDIAP----LQEI 217
Cdd:cd00610 147 KyrgGFGPLLPGVLHVPY-----PYRYRPPAELADDLEA-LEEALEEHPEEVA---AVIVEpiqgegGVIVPppgyLKAL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 218 CCLASRYGALVFMDEChATGFlGPTGR-GTDELLGVM-DqvtIInsTLGKALGGAS--GGYTTGPGPLVSLlrqRARPYL 293
Cdd:cd00610 218 RELCRKHGILLIADEV-QTGF-GRTGKmFAFEHFGVEpD---IV--TLGKGLGGGLplGAVLGREEIMDAF---PAGPGL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 294 FSNSL---PpavVGCA--SKALDLLMgSNTIVQSMAAKTQRFRSKMEAAgftisgASHPICPV-------MLG------- 354
Cdd:cd00610 288 HGGTFggnP---LACAaaLAVLEVLE-EEGLLENAAELGEYLRERLREL------AEKHPLVGdvrgrglMIGielvkdr 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7657118 355 -----DARLASRMADDMLKRGIFVIgfsypvvPKGKARIRVQISAVHSEEDIDRCVEAFVEV 411
Cdd:cd00610 358 atkppDKELAAKIIKAALERGLLLR-------PSGGNVIRLLPPLIITEEEIDEGLDALDEA 412
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
115-410 |
1.06e-10 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 62.74 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 115 LEAKIARFHQR--------EDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAhKYRYRHLD----MA 182
Cdd:cd00609 41 LREAIAEWLGRrggvdvppEEIVVTNGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGA-EVVPVPLDeeggFL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 183 DLEAKLQEAQKHRLRLVA-------TDGAFSMDGdiapLQEICCLASRYGALVFMDECHatGFLGPTGRGTDELLGV-MD 254
Cdd:cd00609 120 LDLELLEAAKTPKTKLLYlnnpnnpTGAVLSEEE----LEELAELAKKHGILIISDEAY--AELVYDGEPPPALALLdAY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 255 QVTIINSTLGKALGGAS--GGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCAsKALDLLMGS-NTIVQSMAAKTQRFR 331
Cdd:cd00609 194 ERVIVLRSFSKTFGLPGlrIGYLIAPPEELLERLKKLLPYTTSGPSTLSQAAAA-AALDDGEEHlEELRERYRRRRDALL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 332 SKMEAAGFTI----SGASHpicpVMLG-----DARLASRMAddmLKRGIFVIGFSYPvVPKGKARIRvqISAVHSEEDID 402
Cdd:cd00609 273 EALKELGPLVvvkpSGGFF----LWLDlpegdDEEFLERLL---LEAGVVVRPGSAF-GEGGEGFVR--LSFATPEEELE 342
|
....*...
gi 7657118 403 RCVEAFVE 410
Cdd:cd00609 343 EALERLAE 350
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
144-237 |
9.38e-06 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 47.44 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 144 ALLTPEDAVLSDELNHASIIDGIR-LCKAHKYRYR--------HLDMADLEAKLQEaqkhRLRLVATDGAFSMDGDIAPL 214
Cdd:COG0520 98 GRLKPGDEILITEMEHHSNIVPWQeLAERTGAEVRvipldedgELDLEALEALLTP----RTKLVAVTHVSNVTGTVNPV 173
|
90 100
....*....|....*....|...
gi 7657118 215 QEICCLASRYGALVFMDECHATG 237
Cdd:COG0520 174 KEIAALAHAHGALVLVDGAQSVP 196
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
146-403 |
1.42e-05 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 46.86 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 146 LTPEDAVLSDELNHASIIDGI-RLCKAHKYRYR--------HLDMADLEAKLqeaqKHRLRLVATDGAFSMDGDIAPLQE 216
Cdd:pfam00266 85 LKPGDEIVITEMEHHANLVPWqELAKRTGARVRvlpldedgLLDLDELEKLI----TPKTKLVAITHVSNVTGTIQPVPE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 217 ICCLASRYGALVFMDECHATG--------------------FLGPTGRG----TDELLGVMDqvtiinstlgKALGGasG 272
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGhrpidvqklgvdflafsghkLYGPTGIGvlygRRDLLEKMP----------PLLGG--G 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118 273 GYTTGPGplVSLLRQRARPYLFSNSLPP--AVVGCAsKALDLLM--GSNTIVQSMAAKTQRFRSKMEAAGFTisgashpi 348
Cdd:pfam00266 229 GMIETVS--LQESTFADAPWKFEAGTPNiaGIIGLG-AALEYLSeiGLEAIEKHEHELAQYLYERLLSLPGI-------- 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7657118 349 cpVMLGDARLASRM---------ADDML---KRGIFVIGFSYPVVPKGKAR-----IRVQISAVHSEEDIDR 403
Cdd:pfam00266 298 --RLYGPERRASIIsfnfkgvhpHDVATlldESGIAVRSGHHCAQPLMVRLglggtVRASFYIYNTQEDVDR 367
|
|
|